Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006531 | biological_process | aspartate metabolic process |
| A | 0006533 | biological_process | L-aspartate catabolic process |
| A | 0006536 | biological_process | glutamate metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016212 | molecular_function | kynurenine-oxoglutarate transaminase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE KET A 412 |
| Chain | Residue |
| A | VAL37 |
| A | GLY38 |
| A | TYR70 |
| A | SER107 |
| A | GLY108 |
| A | THR109 |
| A | TRP140 |
| A | ASN194 |
| A | ASP222 |
| A | TYR225 |
| A | SER255 |
| A | ALA257 |
| A | LYS258 |
| A | ARG266 |
| A | ARG292 |
| A | ARG386 |
| A | HOH467 |
| site_id | ACT |
| Number of Residues | 20 |
| Details | RESIDUES INTERACTING WITH COENZYME-SUBSTRATE ADDUCT |
| Chain | Residue |
| A | ASP15 |
| A | TRP140 |
| A | ASN194 |
| A | ASP222 |
| A | ALA224 |
| A | TYR225 |
| A | SER255 |
| A | LYS258 |
| A | ARG266 |
| A | PHE360 |
| A | ARG386 |
| A | ILE17 |
| A | KET412 |
| A | LEU18 |
| A | VAL37 |
| A | GLY38 |
| A | ALA39 |
| A | SER107 |
| A | GLY108 |
| A | THR109 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYAKnmGLyGERAG |
| Chain | Residue | Details |
| A | SER255-GLY268 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TRP140 | |
| A | ASP222 | |
| A | LYS258 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TRP140 | |
| A | ASP222 | |
